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Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Almelysin, a new metalloproteinase with significant efficiency in low temperatures, is also other proteinase isolated from the culture filtrate of Alteromonas sp. The metalloprotease secreted by Alteromonas sp. is essential in the strain’s chitin degradation pathway. Aeromonas salmonicida subsp. has been found as a protamine-reducing marine bacterium obtained from marine soil. Extremophile hydrolases have benefits over chemical biocatalysts. These catalysts are non- polluting, environmentally acceptable, extremely specific, and occur in mild reaction circumstances. Such hydrolases may activate in the form of organic liquids, which is crucial for the production of single-isomer chiral medicines. These hydrolases have been used in a variety of ways. L-asparaginase is a hydrolase which produces L-aspartic and ammonia from L-asparagine. L-glutaminase activities is also present in this enzyme. Antileukemia/antilymphoma drugs made from microbial L-asparaginase preparations for biomedical applications presently account for one-third of global demand. L-asparaginases have been widely utilized in children particularly its act as chemotherapy for acute lymphoblastic leukemia, which is considerably greater than various therapeutic enzymes. L-asparaginase has been treated as an anti-tumor therapy in non-lymphoma, bovine lymphoma sarcoma, chronic lymphocytic leukemia Hodgkin’s pancreatic carcinoma, lymphosarcoma, lymphosarcoma, reticulum sarcoma, acute myelomonocytic leukemia, melanoma sarcoma and acute myelocytic leukemia.
A Review on L-Asparaginase
Published in Se-Kwon Kim, Marine Biochemistry, 2023
The irreversible conversion of blood glutamine into glutamic acid and ammonia is because of the presence of glutaminase activity of asparaginase. The resulting glutamate reacts with sodium in blood and gives rise to the production of monosodium glutamate (Kurtzberg et al., 2003). There are reports suggesting that due to the presence of glutaminase activity of asparaginase, leukemia patients suffer from many life-threatening side effects, such as leucopenia, acute pancreatitis, immunosuppression, hyperglycemia, thromboembolysis and neurological seizures (Devi et al.,2012; Ramya et al.,2012). Therefore, it is necessary to make a search for glutaminase-free asparaginase from the native microorganisms. In the control of leukemia, the pharmacodynamics of asparaginase differs by formulation (Pinheiro and Boos, 2004). The treatment mainly depends on the intensity of the dose and duration of the treatment of asparaginase rather than the type of asparaginase used (Silverman et al., 2001; Pui and Evans, 2006). Currently, L-asparaginase obtained from Erwinia carotovora and Escherichia coli is of commercial importance. Other microbes, such as Bacillus sp., Corneybacterium glutamicum, Enterobacter sp., Pseudomonas stutzeri and others, also produce a feasible amount of enzyme. As far as fungi are concerned, Aspergillus oryzae was found to synthesis large amount of enzyme.
Konjac Polysaccharide for Drug Delivery
Published in Akhilesh Vikram Singh, Bang-Jing Li, Polysaccharides in Advanced Drug Delivery, 2020
Wei Ha, Sheng Zhang, Yang Kang, Bang-Jing Li
L-asparaginase has been widely used to treat malignant tumors, particularly acute lymphoblastic leukemia (ALL). The growth of malignant tumor cells depends on the introduction of exogenous L-asparagine in most of the patients with ALL[62]. Tumor cells will languish without ingestion of exogenous L-asparagine whereas normal cells can synthesize L-asparagine themselves. L-asparaginase can effectively decrease the content of L-asparagine in blood by converting it to L-aspartic acid and ammonia. Although it has high therapeutic efficacy, there are still some problems that exist in the therapeutic field, such as immunological response and side effects (i.e., fever, skin rashes, allergic reactions and even anaphylactic shocks). In order to improve enzyme efficiency and reduce the immune response and toxicity, Li et al. prepared CKGM-CS nanoparticles as a novel biocompatible matrix system for L-asparaginase immobilization[63]. The preparation of the nanocapsules was completely conducted in water and the immobilized L-asparaginase maintained the original activity of the free enzyme. The encapsulation efficiency reached 68.0% when both the concentrations of CKGM and CS were 0.01% and the particle size was in a range 100–300 nm. Compared with the free L-asparaginase, the immobilized enzyme system showed significantly higher thermostability and had preferable resistance to acid and alkaline environments (Figure 4.7). This study illustrated that the nanocapsules have semi-permeability and can be used to immobilize thermal and pH-sensitive enzymes.
Production, purification and kinetic characterization of glutaminase free anti-leukemic L-asparaginase with low endotoxin level from novel soil isolate
Published in Preparative Biochemistry & Biotechnology, 2020
Pragya Prakash, Hare Ram Singh, Santosh Kumar Jha
Bacterial strains were procured from MTCC, and the soil samples were collected from 6 feet depth from the top surface of soil using a syringe and were serially diluted to a range of 10−1 to 10−10 dilution. Different bacterial strains were isolated on Nutrient Agar medium and were screened for the production of asparaginase. The micro-organisms were maintained at 4 °C, and initial screening for the production of asparaginase was done over modified M9 agar medium. The media comprised of the following: Glucose (1.5 g/L), K2HPO4 (1.2 g/L), NaCl (0.5 g/L), L-asparagine (10 g/L), Agar (20 g/L) and Phenol red 2.5% (1 mL). The pH of the medium was adjusted to 7.4. Bacterial colonies from soil isolates maintained on Nutrient Agar plate were streaked on M9 medium plates and incubated overnight at 37 °C. L-asparagine was used as a sole nitrogen source in the medium.
L-Asparaginase from E. chrysanthemi expressed in glycoswitch®: effect of His-Tag fusion on the extracellular expression
Published in Preparative Biochemistry and Biotechnology, 2019
Brian Effer, Guilherme Meira Lima, Sindy Cabarca, Adalberto Pessoa, Jorge G. Farías, Gisele Monteiro
L-Asparaginase (L-ASNase) is an important enzyme used as a biopharmaceutical product to treat acute lymphoblastic leukemia (ALL) because it catalyzes the conversion of serum asparagine (Asn) to aspartic acid and ammonia, causing the death of leukemic cells by starvation due to lack of Asn for protein synthesis.[1] The commercial versions of the L-ASNase approved by the US Food and Drug Administration (FDA) to treat ALL are derived from bacteria (E. coli: Kidrolase®, EUSA Pharma Inc.; Oncaspar®, Enzon Pharmaceutical Inc.; and E. chrysanthemi: Erwinase®, JZP-416®; EUSA Pharma Inc.) or produced as a recombinant in E. coli expression systems.[2] This prokaryotic system is widely used due to its rapid cell growth, high protein yield, low-cost production medium, and its genome has been well studied.[3] However, bacteria tend to accumulate lipopolysaccharide in their outer membrane (which is immunogenic in humans)[4] and methods to produce extracellular proteins have still not been entirely described,[5] resulting in either cytoplasmic or periplasmic production, which requires cell lysis and further recombinant protein purification. In addition, a high expression rate can produce protein in insoluble inclusion bodies, thereby requiring extra steps to fold recombinant active proteins.
Extracellular L-asparaginase production in solid-state fermentation by using sugarcane bagasse as support material
Published in Preparative Biochemistry and Biotechnology, 2019
J. J. Muso Cachumba, R. Terán Hilares, L. P. Brumano, P. R. F. Marcelino, F. A. F. Antunes, J. C. Santos, S. S. da Silva
L-asparaginase (L-asparagine amino hydrolase, E.C.3.5.1.1) is an enzyme that catalyzes the hydrolysis of L-asparagine to L-aspartate and ammonia.[1] In the food industry, L-asparaginase is used for the reduction of acrylamide formation in heated food without altering their physicochemical and sensorial characteristics.[1,2] Also, in pharmaceutical industry, this enzyme is mainly used for the treatment of acute lymphoblastic leukemia (ALL), due to its antitumor agent property.[3] Considering the importance and applications of this enzyme, the interest in its production has increased, and hence, microorganisms such as bacteria, fungi, and yeasts have been applied for this purpose.[3] However, for antitumor application of bacterial L-asparaginases, some problems as hypersensitivity and immune inactivation were reported, mainly because they are produced by a prokaryotic microorganism.[4] Moreover, other related secondary effects are allergic reaction, pancreatitis, diabetes, and coagulation problems. Thus, due to better compatibility with the human system, eukaryotic microorganisms such as filamentous fungi and yeasts have been evaluated as interesting alternatives.[3,5]